Mitogen-activated protein kinase 9

Today we want to talk about Mitogen-activated protein kinase 9. It is an issue that concerns us all, since it has a direct impact on our lives. Mitogen-activated protein kinase 9 is a topic that has been present throughout history and has sparked endless debates and reflections, both in the academic field and in society in general. It is a topic that does not leave anyone indifferent, since its implications are diverse and its consequences can be significant. Therefore, it is important to dedicate time and effort to understanding and analyzing Mitogen-activated protein kinase 9, in order to make informed decisions and contribute to the debate around this very relevant topic.

MAPK9
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesMAPK9, JNK-55, JNK2, JNK2A, JNK2ALPHA, JNK2B, JNK2BETA, PRKM9, SAPK, SAPK1a, p54a, p54aSAPK, mitogen-activated protein kinase 9
External IDsOMIM: 602896; MGI: 1346862; HomoloGene: 55685; GeneCards: MAPK9; OMA:MAPK9 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

5601

26420

Ensembl

ENSG00000050748

ENSMUSG00000020366

UniProt

P45984

Q9WTU6

RefSeq (mRNA)

NM_001163671
NM_001163672
NM_016961
NM_207692

RefSeq (protein)

NP_001157143
NP_001157144
NP_058657
NP_997575

Location (UCSC)Chr 5: 180.23 – 180.29 MbChr 11: 49.74 – 49.78 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Mitogen-activated protein kinase 9 is an enzyme that in humans is encoded by the MAPK9 gene.[5]

Function

The protein encoded by this gene is a member of the MAP kinase family. MAP kinases act as an integration point for multiple biochemical signals, and are involved in a wide variety of cellular processes such as proliferation, differentiation, transcription regulation and development. This kinase targets specific transcription factors, and thus mediates immediate-early gene expression in response to various cell stimuli. It is most closely related to MAPK8, both of which are involved in UV radiation-induced apoptosis, thought to be related to the cytochrome c-mediated cell death pathway. This gene and MAPK8 are also known as c-Jun N-terminal kinases. This kinase blocks the ubiquitination of tumor suppressor p53, and thus it increases the stability of p53 in nonstressed cells. Studies of this gene's mouse counterpart suggest a key role in T-cell differentiation. Four alternatively spliced transcript variants encoding distinct isoforms have been reported.[6]

Interactions

Mitogen-activated protein kinase 9 has been shown to interact with:

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000050748 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000020366 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Kallunki T, Su B, Tsigelny I, Sluss HK, Dérijard B, Moore G, Davis R, Karin M (Dec 1994). "JNK2 contains a specificity-determining region responsible for efficient c-Jun binding and phosphorylation". Genes & Development. 8 (24): 2996–3007. doi:10.1101/gad.8.24.2996. PMID 8001819.
  6. ^ "Entrez Gene: MAPK9 mitogen-activated protein kinase 9".
  7. ^ Saleem A, Datta R, Yuan ZM, Kharbanda S, Kufe D (Dec 1995). "Involvement of stress-activated protein kinase in the cellular response to 1-beta-D-arabinofuranosylcytosine and other DNA-damaging agents". Cell Growth & Differentiation. 6 (12): 1651–8. PMID 9019171.
  8. ^ Kharbanda S, Saleem A, Shafman T, Emoto Y, Taneja N, Rubin E, Weichselbaum R, Woodgett J, Avruch J, Kyriakis J (Aug 1995). "Ionizing radiation stimulates a Grb2-mediated association of the stress-activated protein kinase with phosphatidylinositol 3-kinase". The Journal of Biological Chemistry. 270 (32): 18871–4. doi:10.1074/jbc.270.32.18871. PMID 7642542.
  9. ^ a b Yasuda J, Whitmarsh AJ, Cavanagh J, Sharma M, Davis RJ (Oct 1999). "The JIP group of mitogen-activated protein kinase scaffold proteins". Molecular and Cellular Biology. 19 (10): 7245–54. doi:10.1128/mcb.19.10.7245. PMC 84717. PMID 10490659.
  10. ^ Whitmarsh AJ, Cavanagh J, Tournier C, Yasuda J, Davis RJ (Sep 1998). "A mammalian scaffold complex that selectively mediates MAP kinase activation". Science. 281 (5383): 1671–4. Bibcode:1998Sci...281.1671W. doi:10.1126/science.281.5383.1671. PMID 9733513.
  11. ^ Ito M, Yoshioka K, Akechi M, Yamashita S, Takamatsu N, Sugiyama K, Hibi M, Nakabeppu Y, Shiba T, Yamamoto KI (Nov 1999). "JSAP1, a novel jun N-terminal protein kinase (JNK)-binding protein that functions as a Scaffold factor in the JNK signaling pathway". Molecular and Cellular Biology. 19 (11): 7539–48. doi:10.1128/mcb.19.11.7539. PMC 84763. PMID 10523642.
  12. ^ Kelkar N, Gupta S, Dickens M, Davis RJ (Feb 2000). "Interaction of a mitogen-activated protein kinase signaling module with the neuronal protein JIP3". Molecular and Cellular Biology. 20 (3): 1030–43. doi:10.1128/mcb.20.3.1030-1043.2000. PMC 85220. PMID 10629060.
  13. ^ Hu MC, Qiu WR, Wang YP (Nov 1997). "JNK1, JNK2 and JNK3 are p53 N-terminal serine 34 kinases". Oncogene. 15 (19): 2277–87. doi:10.1038/sj.onc.1201401. PMID 9393873.
  14. ^ Lin Y, Khokhlatchev A, Figeys D, Avruch J (Dec 2002). "Death-associated protein 4 binds MST1 and augments MST1-induced apoptosis". The Journal of Biological Chemistry. 277 (50): 47991–8001. doi:10.1074/jbc.M202630200. PMID 12384512.
  15. ^ Maekawa M, Nishida E, Tanoue T (Oct 2002). "Identification of the Anti-proliferative protein Tob as a MAPK substrate". The Journal of Biological Chemistry. 277 (40): 37783–7. doi:10.1074/jbc.M204506200. PMID 12151396.

Further reading

This article incorporates text from the United States National Library of Medicine, which is in the public domain.